We plan to prepare low D.S. chemically altered amylose such as 6-fluoro, 6-deoxy, 2-deoxy as substrates for porcine pancreatic amylase. After exhaustive amylase action on these substrates we will isolate the products containing modified glucose units and determine their structures. From this information we can deduce the roles of the various OH groups in the substrate on enzyme binding and catalysis. Gluconolactone and maltobionic acid lactone are putative transition state analogs and are known to inhibit amylases. We will prepare lactones of higher oligosaccharides to use as inhibitors in order to definitely locate the position of the lactone residue at the enzyme's substrate binding site. If the compounds are strongly inhibitory, we will determine the type of inhibition and inhibitor constants. We plan to probe the mechanism of B. macerans transglycosylase ("amylase") by using amylose as glycosyl donor and radioactive glucose as acceptor, then we will determine the structures of the products. UDPG* as well as ADPG* will be used as glucosyl donors for granule-bound starch synthetase to elucidate the role of the granule-bound enzyme in amylose biosynthesis (amylopectin biosynthesis in waxy maize does not require granule-bound synthetase and can not utilize UDPG as a glucosyl donor).